1VR7
Crystal structure of S-adenosylmethionine decarboxylase proenzyme (TM0655) from THERMOTOGA MARITIMA at 1.2 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004014 | molecular_function | adenosylmethionine decarboxylase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006596 | biological_process | polyamine biosynthetic process |
| A | 0008295 | biological_process | spermidine biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0004014 | molecular_function | adenosylmethionine decarboxylase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006596 | biological_process | polyamine biosynthetic process |
| B | 0008295 | biological_process | spermidine biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 131 |
| Chain | Residue |
| A | VAL9 |
| A | GLU11 |
| A | HIS106 |
| B | HIS110 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Schiff-base intermediate with substrate; via pyruvic acid","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor; for processing activity","evidences":[{"source":"PubMed","id":"15150268","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor; for catalytic activity","evidences":[{"source":"PubMed","id":"15150268","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Cleavage (non-hydrolytic); by autolysis","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Pyruvic acid (Ser); by autocatalysis","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details |
| Chain | Residue | Details |
| A | HIS68 | |
| A | CYS83 | |
| A | SER55 | |
| A | SER63 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details |
| Chain | Residue | Details |
| B | HIS68 | |
| B | CYS83 | |
| B | SER55 | |
| B | SER63 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 225 |
| Chain | Residue | Details |
| A | ILE67 | electrostatic stabiliser |
| A | GLY74 | covalently attached, electrophile, hydrogen bond acceptor, hydrogen bond donor, proton acceptor |
| A | TYR75 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleophile, polar interaction, proton donor |
| A | LEU80 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | HIS95 | hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 225 |
| Chain | Residue | Details |
| B | ILE67 | electrostatic stabiliser |
| B | GLY74 | covalently attached, electrophile, hydrogen bond acceptor, hydrogen bond donor, proton acceptor |
| B | TYR75 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleophile, polar interaction, proton donor |
| B | LEU80 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | HIS95 | hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor |
